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Templates That Induce α-Helical, β-Sheet, and Loop Conformations

机译:产生α-螺旋,β-Sheet和环构象的模板

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摘要

Polypeptides composed of 30 amino acid residues or less typically do not adopt well-defined conformations in aqueous solution; rather they adopt an ensemble of energetically similar conformations. The small free energy difference (3-15 kcal/mol) that stabilizes the folded state of a native protein over the unfolded state is difficult to achieve in a small polypeptide as the difference in free energy between the folded and unfolded state is derived from the difference between two large numbers representing entropic and enthalpic contributions from both the solvent and the polypeptide chain.
机译:由30个或更少氨基酸残基组成的多肽通常在水溶液中不具有明确定义的构象;相反,他们采用了在能量上类似的整体结构。在小的多肽中很难实现稳定天然蛋白质在未折叠状态的折叠状态的小自由能差(3-15 kcal / mol),因为折叠和未折叠状态之间的自由能差源自于代表溶剂和多肽链的熵和焓贡献的两个大数之差。

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